Abstract
F1Fo ATP synthase is present in all life and is responsible for the production of almost all adenosine triphosphate (ATP), which is one of the most prolific energy molecules that are synthesized during metabolism. Fo converts electrochemical potential into mechanical rotation, which drives conformational changes in F1 that facilitate the synthesis of ATP. The mechanism of rotation of the subunit c ring is not clear. This study looked for evidence of the ratcheting mechanism of rotation, which states that the helices of the subunit a-c interface act like mechanical gears during rotation. Site-directed mutagenesis was used to mutate aV71C, which is located on a loop of subunit a. This mutant ATP synthase was purified and then chemically modified with a spin label, which can be observed using electron paramagnetic resonance (EPR) spectroscopy. The EPR signal is sensitive to the protein environment and will provide data on the mobility of the residue to which the spin label is attached. The presence of free spin and spin dimers was too strong to allow for interpretation of the mobility of aV71C. The quality of the data needs to be improved by optimization of the purification technique.
How to Cite
Stowe, R., (2018) “Spectroscopic Study Of Conformational Changes In The a Subunit of F1Fo ATP Synthase”, Capstone, The UNC Asheville Journal of Undergraduate Scholarship 31(1).
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